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Open-form crystal structure of human ryr receptor 3 ( 848-1055)

Analyse Open-form crystal structure of human ryr receptor 3 ( 848-1055) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UHA
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ryanodine receptor 3
UniProt: Q15413
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Ryanodine receptor 3	protein	206	48% helix, 9% strand	Q15413
A	Ryanodine receptor 3	protein	206	44% helix, 9% strand	Q15413

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	446	0.67	0.79	45	empty
2	471	0.63	0.76	51	empty
3	162	0.42	0.74	19	empty

Interfaces

1 interface between chains.

B–A · 354 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

6UHA · Open-form Crystal Structure of Human RYR Receptor 3 ( 848-1055) · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q15413
Elsewhere: RCSB PDB 6UHA · PDBe 6UHA · UniProt Q15413

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